An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase

Gabrielle N. Thibodeaux; Wilfred A. van der Donk

doi:10.1039/c2cc34138g

An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase

Gabrielle N. Thibodeaux, Wilfred A. van der Donk

Research output: Contribution to journal › Article › peer-review

Abstract

Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo.

Original language	English (US)
Pages (from-to)	10615-10617
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	86
DOIs	https://doi.org/10.1039/c2cc34138g
State	Published - Oct 3 2012

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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abstract = "Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo.",

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AB - Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo.

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An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase

Abstract

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